B. Entsch

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Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis.

M. Ortiz-Maldonado, B. Entsch, D. Ballou, 2004, Biochemistry.

Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase.

M. Ortiz-Maldonado, B. Entsch, D. Ballou, 2010, Biochemistry.

Protonation status and control mechanism of flavin–oxygen intermediates in the reaction of bacterial luciferase

N. Lawan, P. Chaiyen, R. Tinikul, 2020, The FEBS journal.

LuxG Is a Functioning Flavin Reductase for Bacterial Luminescence

P. Chaiyen, B. Entsch, D. Ballou, 2007, Journal of bacteriology.

Substrate recognition by "password" in p-hydroxybenzoate hydroxylase.

B. Entsch, D. Ballou, V. Massey, 1999, Biochemistry.

Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant.

K. K. Frederick, B. Entsch, D. Ballou, 2002, Biochemistry.

An Improved Method for Measuring the CO2/O2 Specificity of Ribulosebisphosphate Carboxylase-Oxygenase

M. Morell, B. Entsch, H. Kane, 1994 .

Kinetic Mechanisms of the Oxygenase from a Two-component Enzyme, p-Hydroxyphenylacetate 3-Hydroxylase from Acinetobacter baumannii*

P. Chaiyen, B. Entsch, D. Ballou, 2006, Journal of Biological Chemistry.

Phosphorus and nitrogen in coral reef sediments

B. Entsch, K. Boto, R. Sim, 1983 .

Mass spectrometric identification of indole compounds produced by Rhizobium strains

C. W. Parker, B. Rolfe, R. Summons, 1982 .

Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase.

P. Chaiyen, B. Entsch, D. Ballou, 2007, Biochemistry.

Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.

B. Entsch, D. Ballou, Lindsay J Cole, 2005, Archives of biochemistry and biophysics.

The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis.

P. Chaiyen, B. Entsch, D. Ballou, 2005, Biochemistry.

Properties of p-hydroxybenzoate hydroxylase when stabilized in its open conformation.

M. Ortiz-Maldonado, B. Entsch, D. Ballou, 2005, Biochemistry.

On the structure of flavin-oxygen intermediates involved in enzymatic reactions.

S. Ghisla, B. Entsch, V. Massey, 1977, European journal of biochemistry.

An enzyme from lupin seeds forming alanine derivatives of cytokinins

C. W. Parker, B. Entsch, D. Letham, 1983 .

Preparation and characterization, using high-performance liquid chromatography, of an enzyme forming glucosides of cytokinins.

C. W. Parker, R. Summons, B. Entsch, 1979, Biochimica et biophysica acta.

Monitoring Changing Toxigenicity of a Cyanobacterial Bloom by Molecular Methods

D. Mckay, B. Neilan, B. Entsch, 2002, Applied and Environmental Microbiology.

Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa.

B. Entsch, K. F. Scott, K. Weaich, 1988, Gene.

Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase.

V Massey, B. Entsch, D. Ballou, 1976, The Journal of biological chemistry.

Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases.

B. Entsch, D. Ballou, Lindsay J Cole, 2005, Biochemical and biophysical research communications.

Analysis of the pobA and pobR genes controlling expression of p-hydroxybenzoate hydroxylase in Azotobacter chroococcum.

D. Mckay, B. Entsch, J. A. Quinn, 2001, Gene.

[24] Hydroxybenzoate hydroxylase

B. Entsch, 1990 .

Purification, properties, and oxygen reactivity of p-hydroxybenzoate hydroxylase from Pseudomonas aeruginosa.

B. Entsch, D. Ballou, 1989, Biochimica et biophysica acta.

Oxygen reactivity of p-hydroxybenzoate hydroxylase containing 1-deaza-FAD.

C. Walsh, B. Entsch, D. Ballou, 1980, The Journal of biological chemistry.

Identification of cyanobacteria and their toxigenicity in environmental samples by rapid molecular analysis

D. Mckay, B. Neilan, B. Entsch, 2001, Environmental toxicology.

Fluoride elimination from substrates in hydroxylation reactions catalyzed by p-hydroxybenzoate hydroxylase.

P. Chapman, B. Entsch, D. Ballou, 1980, The Journal of biological chemistry.

Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase.

P. Chaiyen, B. Entsch, D. Ballou, 2004, Biochemistry.

Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover.

M. Ortiz-Maldonado, B. Entsch, D. Ballou, 2004, Biochemistry.

The purification and identification of flavin nucleotides by high-performance liquid chromatography.

B. Entsch, R. Sim, 1983, Analytical biochemistry.

Metabolites of Cytokinins

C. W. Parker, R. Summons, B. Entsch, 1980 .

The mobile flavin of 4-OH benzoate hydroxylase.

M. Lah, M. Ludwig, D. Gatti, 1994, Science.

Catalytic function of tyrosine residues in para-hydroxybenzoate hydroxylase as determined by the study of site-directed mutants.

B. Entsch, D. Ballou, V. Massey, 1991, The Journal of biological chemistry.

Regulators of cell division in plant tissues

R. Summons, B. Entsch, J. Macleod, 1980, Planta.

Glucosylation of cytokinin analogues

C. W. Parker, R. Summons, B. Entsch, 1978 .

Mass spectrometric analysis of cytokinins in plant tissues. II—Quantitation of cytokinins in Zea mays kernels using deuterium labelled standards

C. W. Parker, R. Summons, B. Entsch, 1979 .

Enzymic glucosylation of the cytokinin, 6-benzylaminopurine

B. Entsch, D. Letham, 1979 .

Cytokinin Translocation and Metabolism in Species of the Leguminoseae: Studies in Relation to Shoot and Nodule Development

C. W. Parker, B. Rolfe, R. Summons, 1981 .

Mass spectrometric analysis of cytokinins in plant tissues

C. W. Parker, R. Summons, B. Entsch, 1979 .

Inhibitors of two enzymes which metabolize cytokinins

C. W. Parker, B. Entsch, D. Letham, 1986 .

Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata.

R. E. Wicks, B. Entsch, 1993, Biochemical and biophysical research communications.

Occurrence and expression of members of the ferritin gene family in cowpeas.

R. E. Wicks, B. Entsch, A. J. Wardrop, 1999, The Biochemical journal.

Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase

D. Gatti, M. Ortiz-Maldonado, B. Entsch, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The reaction mechanisms of groups A and B flavoprotein monooxygenases

B. Entsch, D. Ballou, 2013 .

Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologues.

P. Chaiyen, B. Entsch, D. Ballou, 2007, Journal of biochemistry.

The cyanobiont in an Azolla fern is neither Anabaena nor Nostoc.

D. Mckay, B. Entsch, Judith A Baker, 2003, FEMS microbiology letters.

Intermediates in flavoprotein catalyzed hydroxylations.

B. Entsch, D. Ballou, V. Massey, 1974, Biochemical and biophysical research communications.

Changes in the catalytic properties of p-hydroxybenzoate hydroxylase caused by the mutation Asn300Asp.

B. Entsch, D. Ballou, V. Massey, 1994, Biochemistry.

Conformational dynamics of the isoalloxazine in substrate-free p-hydroxybenzoate hydroxylase: single-molecule studies.

J. Brender, B. Entsch, D. Ballou, 2005, Journal of the American Chemical Society.

CHEMICAL FUNCTIONS OF AMINO ACID RESIDUES IN THE ACTIVE SITE OF PARAHYDROXYBENZOATE HYDROXYLASE AS STUDIED BY SITE DIRECTED MUTAGENESIS AND BIOPHYSICAL TECHNIQUES

B. Entsch, D. Ballou, V. Massey, 1991 .

Flavin‐Mediated Hydroxylation Reactions

B. Entsch, D. Ballou, 2008 .

para-Hydroxybenzoate hydroxylase containing 6-hydroxy-FAD is an effective enzyme with modified reaction mechanisms.

B. Entsch, V. Massey, A. Claiborne, 1987, The Journal of biological chemistry.

Hydroxybenzoate hydroxylase.

B. Entsch, 1990, Methods in Enzymology.

pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis.

M. Ludwig, D. Gatti, B. Entsch, 1996, Biochemistry.

Removal of a methyl group causes global changes in p-hydroxybenzoate hydroxylase.

D. Gatti, B. Entsch, D. Ballou, 2005, Biochemistry.

A gene, cobA + hemD, from Selenomonas ruminantium encodes a bifunctional enzyme involved in the synthesis of vitamin B12.

B. Entsch, P. Anderson, David McKay, 2001, Gene.

Nicotinamide adenine dinucleotide phosphate photoreduction from water by agranal chloroplasts isolated from bundle sheath cells of maize.

D. G. Bishop, R. Smillie, B. Entsch, 1972, Plant physiology.